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The crystal structure of the complex between hen egg lysozyme and the Fv fragment of a humanized antilysozyme antibody was determined to 2.7-Å resolution. The structure of the antigen combining site in the complex is nearly identical to that of the complexed form of the parent mouse antibody, D1.3. In contrast, the combining sites of the unliganded mouse and humanized antilysozymes show moderate conformational differences. This disparity suggests that a conformational readjustment process linked to antigen binding reverses adverse conformations in the complementarity determining regions that had been introduced by engineering these segments next to human framework regions in the humanized antibody.
We gratefully acknowledge financial support from the Arnold and Mabel Beckman Foundation and the Department of the Army Breast Cancer Research Program (grant DAMD 17-97-1-7124).
Address correspondence to Jefferson Foote, Division of Molecular Medicine, Fred Hutchinson Cancer Research Center, 1100 Fairview Ave. North, C3-168, PO Box 19024, Seattle, WA 98109-1024. Phone: 1-206-667-6720; Fax: 1-206-667-6524; E-mail: jfoote{at}fhcrc.org
1 Abbreviations used in this paper: C
, alpha carbon; CDR, complementarity determining region; Fv, dimer of immunoglobulin heavy and light chain variable domains; rms, root mean square.
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